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  Domain Name: metallo-dependent_hy
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 35
Total Disease Mutations Found: 27
This domain occurred 14 times on human genes (35 proteins).



  ADENOSINE DEAMINASE DEFICIENCY, PARTIAL
  B CELL-NEGATIVE, NK CELL-NEGATIVE, DUE TO ADENO
  ERYTHROCYTE AMP DEAMINASE DEFICIENCY
  MYOPATHY DUE TO MYOADENYLATE DEAMINASE DEFICIENCY
  RECLASSIFIED - VARIANT OF UNKNOWN SIGNIFICANCE
  SEVERE COMBINED IMMUNODEFICIENCY, AUTOSOMAL RECESSIVE, T CELL-NEGATIVE,


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   Protein ID            Protein Position

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Feature Name:Total Found:
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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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